Helical peptoid mimics of lung surfactant protein C |
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Authors: | Wu Cindy W Seurynck Shannon L Lee Ka Yee C Barron Annelise E |
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Institution: | Department of Chemical Engineering, Northwestern University, 2145 Sheridan Road, Room E136, Evanston, IL 60208, USA. |
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Abstract: | Among the families of peptidomimetic foldamers under development as novel biomaterials and therapeutics, poly-N-substituted glycines (peptoids) with alpha-chiral side chains are of particular interest for their ability to adopt stable, helical secondary structure in organic and aqueous solution. Here, we show that a peptoid 22-mer with a biomimetic sequence of side chains and an amphipathic, helical secondary structure acts as an excellent mimic of surfactant protein C (SP-C), a small protein that plays an important role in surfactant replacement therapy for the treatment of neonatal respiratory distress syndrome. When integrated into a lipid film, the helical peptoid SP mimic captures the essential surface-active behaviors of the natural protein. This work provides an example of how an abiological oligomer that closely mimics both the hydrophobic/polar sequence patterning and the fold of a natural protein can also mimic its biophysical function. |
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